GTP contains chemical energy stored in its high-energy phosphate bonds. It releases energy when it is broken down (hydrolyzed) into GDP (guanosine diphosphate). This energy is used for many metabolic processes, such as gluconeogenesis and protein synthesis.
GTP-binding protein regulators regulate G proteins in several different ways. Small GTPases act as molecular switches in signaling pathways, which act to regulate functions of other proteins. They are active when it is bound to GTP and inactive when bound to GDP. Activation and deactivation of small GTPases can be regarded as occurring in a cycle, between the GTP-bound and GDP-bound form, regulated by other regulatory proteins
The rate of GTP hydrolysis for small GTPases is generally too slow to create physiologically relevant transient signals, and thus requires another class of regulatory proteins to accelerate this activity, the GTPase activating proteins
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